1J1E

Crystal structure of the 52kDa domain of human cardiac troponin in the Ca2+ saturated form

Summary for 1J1E

• Entry DOI: 10.2210/pdb1j1e/pdb
• Related: 1J1D
• Descriptor: Troponin C, Troponin T, Troponin I, ... (4 entities in total)
• Functional Keywords: thin filament, muscle regulation, ca2+ binding protein, ef-hand, coiled-coil, contractile protein
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 6
• Total formula weight: 104220.78

Authors

Takeda, S.,Yamashita, A.,Maeda, K.,Maeda, Y. (deposition date: 2002-12-03, release date: 2003-07-15, Last modification date: 2023-10-25)

Primary citation

Takeda, S.,Yamashita, A.,Maeda, K.,Maeda, Y.
Structure of the core domain of human cardiac troponin in the Ca2+-saturated form
Nature, 424:35-41, 2003

PubMed Abstract: Troponin is essential in Ca(2+) regulation of skeletal and cardiac muscle contraction. It consists of three subunits (TnT, TnC and TnI) and, together with tropomyosin, is located on the actin filament. Here we present crystal structures of the core domains (relative molecular mass of 46,000 and 52,000) of human cardiac troponin in the Ca(2+)-saturated form. Analysis of the four-molecule structures reveals that the core domain is further divided into structurally distinct subdomains that are connected by flexible linkers, making the entire molecule highly flexible. The alpha-helical coiled-coil formed between TnT and TnI is integrated in a rigid and asymmetric structure (about 80 angstrom long), the IT arm, which bridges putative tropomyosin-anchoring regions. The structures of the troponin ternary complex imply that Ca(2+) binding to the regulatory site of TnC removes the carboxy-terminal portion of TnI from actin, thereby altering the mobility and/or flexibility of troponin and tropomyosin on the actin filament.

PubMed: 12840750
DOI: 10.1038/nature01780

Experimental method

X-RAY DIFFRACTION (3.3 Å)